Conservation of a common motif in enzymes catalyzing ADP-ribose transfer. Identification of domains in mammalian transferases.

@article{Takada1995ConservationOA,
  title={Conservation of a common motif in enzymes catalyzing ADP-ribose transfer. Identification of domains in mammalian transferases.},
  author={Tatsuyuki Takada and Katsuyuki Iida and Joel Moss},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 2},
  pages={541-4}
}
Bacterial toxin ADP-ribosyltransferases, e.g. diphtheria toxin (DT) and pertussis toxin, have in common consensus sequences involved in catalytic activity, which are localized to three regions. Region I is notable for a histidine or arginine; region II, approximately 50-75 amino acids downstream, is rich in aromatic/hydrophobic amino acids; and region III, further downstream, has a glutamate and other acidic amino acids. A similar motif was observed in the sequence of the… CONTINUE READING

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